Summary
Evidence is presented for a carbohydrate-binding property of aprotinin, which is preserved both in a fluorescein isothiocyanate (FITC) conjugate and a cyanogen bromidelinked Sepharose conjugate of the protein. Both conjugates similarly retain their tryptic and chymotryptic inhibitory properties. The FITC conjugate is shown to be a single species with respect to charge and to molecular weight and shows a specific binding of normal materials containing sialosyl or uronosyl groups, which accords with its histochemical behaviour. The Sepharose-conjugate showed a similar specificity.
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R.W.S. holds a grant from the Cancer Research Campaign. We thank Dr. G. M. W. Cook for discussion and advice.
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Stoddart, R.W., Kiernan, J.A. Aprotinin, a carbohydrate-binding protein. Histochemie 34, 275–280 (1973). https://doi.org/10.1007/BF00306299
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DOI: https://doi.org/10.1007/BF00306299